Identification and Characterization of New Molecular Partners for the Protein Arginine Methyltransferase 6 (PRMT6)
Figure 5
HMGA1a modulates the methyltransferase activity of PRMT6 toward MIF.
(A) Constant amount of GST-MIF were incubated with recombinant GST-PRMT6 and radio-labelled S-adenosyl-L-(methyl-3H) methionine in the presence of increasing amounts of full length HMGA1 (FL), a truncated HMGA1a form (1–51), and a HMGA1a mutated form (R57,59A) for in vitro methylation assays. Methylation reactions of MIF and HMGA1a alone represent control experiments. Proteins were separated by SDS-PAGE (T = 15%) and checked by fluorography. Experiments were repeated at least twice and a representative result is shown. (B) Blue Comassie staining was used to check for the quantification of HMGA1a proteins. (C) Schematic representation of the FL, 1–51 and R57,59A HMGA1a domain organization.